lnu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Actomyosin based contraction: one mechanokinetic model from single molecules to muscle?
Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences. (bio-nano group)ORCID iD: 0000-0002-5889-7792
2016 (English)In: Journal of Muscle Research and Cell Motility, ISSN 0142-4319, E-ISSN 1573-2657Article in journal (Refereed) Epub ahead of print
Abstract [en]

Bridging the gaps between experimental systems on different hierarchical scales is needed to overcome remaining challenges in the understanding of muscle contraction. Here, a mathematical model with well-characterized structural and biochemical actomyosin states is developed to that end. We hypothesize that this model accounts for generation of force and motion from single motor molecules to the large ensembles of muscle. In partial support of this idea, a wide range of contractile phenomena are reproduced without the need to invoke cooperative interactions or ad hoc states/transitions. However, remaining limitations exist, associated with ambiguities in available data for model definition e.g.: (1) the affinity of weakly bound cross-bridges, (2) the characteristics of the cross-bridge elasticity and (3) the exact mechanistic relationship between the force-generating transition and phosphate release in the actomyosin ATPase. Further, the simulated number of attached myosin heads in the in vitro motility assay differs several-fold from duty ratios, (fraction of strongly attached ATPase cycle times) derived in standard analysis. After addressing the mentioned issues the model should be useful in fundamental studies, for engineering of myosin motors as well as for studies of muscle disease and drug development.

Place, publisher, year, edition, pages
2016.
National Category
Biophysics
Research subject
Natural Science, Biomedical Sciences
Identifiers
URN: urn:nbn:se:lnu:diva-61460DOI: 10.1007/s10974-016-9458-0OAI: oai:DiVA.org:lnu-61460DiVA: diva2:1082878
Available from: 2017-03-19 Created: 2017-03-19 Last updated: 2017-03-23Bibliographically approved

Open Access in DiVA

fulltext(1188 kB)2 downloads
File information
File name FULLTEXT01.pdfFile size 1188 kBChecksum SHA-512
a4bf05e3e3e48a14e94ae07bc53429985da4ae3692510d10205f1dbaa23447f9a455415c78cf5edf2c7e7a99fe38835363996cf522787c57548768a5740e4927
Type fulltextMimetype application/pdf

Other links

Publisher's full text

Search in DiVA

By author/editor
Månsson, Alf
By organisation
Department of Chemistry and Biomedical Sciences
In the same journal
Journal of Muscle Research and Cell Motility
Biophysics

Search outside of DiVA

GoogleGoogle Scholar
Total: 2 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 11 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf